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Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at M phase

Kengo Okamoto1, Noriyuki Sagata

  • 1Department of Biology, Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1, Fukuoka 812-8581, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|March 16, 2007
PubMed

Insights

The Wee-box in Xenopus Wee1 kinase is crucial for its activity. Phosphorylation of a specific motif by Cdc2 at M phase recruits Pin1, leading to Wee1 inactivation during cell division.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Wee1 kinase regulates the cell cycle by inhibiting cyclin B/Cdc2.
  • Wee1 undergoes inactivation at M phase, but the mechanism remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of Wee1 kinase inactivation at M phase.
  • To identify regulatory regions and interactions involved in Wee1 function.

Main Methods:

  • Utilized Xenopus egg and extract systems.
  • Investigated the role of the N-terminal Wee-box and the Thr-186-Pro motif.
  • Assessed the interaction with Pin1.

Main Results:

  • The N-terminal Wee-box is essential for Wee1 kinase activity during interphase.
  • A Thr-186-Pro motif within the Wee-box is phosphorylated by Cdc2 at M phase.
  • This phosphorylated motif binds Pin1, which is required for Wee1 inactivation.

Conclusions:

  • Wee1 inactivation at M phase involves Pin1-mediated isomerization of the phospho-Thr-186-Pro motif.
  • This interaction impairs Wee-box function, leading to catalytic inactivation.
  • Provides novel insights into cell cycle regulation by Wee1.

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